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Protein

Formimidoylglutamase

Gene

hutG

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide.UniRule annotation

Cofactori

Mn2+UniRule annotationNote: Binds 2 manganese ions per subunit.UniRule annotation

Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from N-formimidoyl-L-glutamate (hydrolase route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Formimidoylglutamase (hutG)
This subpathway is part of the pathway L-histidine degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from N-formimidoyl-L-glutamate (hydrolase route), the pathway L-histidine degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi127Manganese 1UniRule annotation1
Metal bindingi157Manganese 1UniRule annotation1
Metal bindingi157Manganese 2UniRule annotation1
Metal bindingi159Manganese 2UniRule annotation1
Metal bindingi161Manganese 1UniRule annotation1
Metal bindingi254Manganese 1UniRule annotation1
Metal bindingi254Manganese 2UniRule annotation1
Metal bindingi256Manganese 2UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Histidine metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciVCHO:VC1204-MONOMER.
UniPathwayiUPA00379; UER00552.

Names & Taxonomyi

Protein namesi
Recommended name:
FormimidoylglutamaseUniRule annotation (EC:3.5.3.8UniRule annotation)
Alternative name(s):
FormiminoglutamaseUniRule annotation
Formiminoglutamate hydrolaseUniRule annotation
Gene namesi
Name:hutGUniRule annotation
Ordered Locus Names:VC_1204
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001737791 – 336FormimidoylglutamaseAdd BLAST336

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1204.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 22Combined sources6
Helixi26 – 29Combined sources4
Beta strandi30 – 32Combined sources3
Helixi35 – 40Combined sources6
Beta strandi45 – 51Combined sources7
Helixi54 – 58Combined sources5
Helixi65 – 67Combined sources3
Helixi68 – 77Combined sources10
Beta strandi87 – 94Combined sources8
Helixi100 – 114Combined sources15
Turni115 – 117Combined sources3
Beta strandi120 – 126Combined sources7
Helixi129 – 143Combined sources15
Beta strandi151 – 156Combined sources6
Beta strandi168 – 170Combined sources3
Helixi179 – 190Combined sources12
Beta strandi195 – 201Combined sources7
Turni203 – 205Combined sources3
Helixi208 – 216Combined sources9
Beta strandi220 – 223Combined sources4
Helixi224 – 226Combined sources3
Turni229 – 231Combined sources3
Helixi232 – 244Combined sources13
Beta strandi247 – 254Combined sources8
Helixi255 – 257Combined sources3
Turni260 – 262Combined sources3
Beta strandi265 – 268Combined sources4
Beta strandi270 – 272Combined sources3
Helixi276 – 288Combined sources13
Turni290 – 292Combined sources3
Beta strandi293 – 299Combined sources7
Helixi303 – 305Combined sources3
Helixi310 – 332Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XFKX-ray1.80A1-336[»]
ProteinModelPortaliQ9KSQ2.
SMRiQ9KSQ2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KSQ2.

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG41088SP. Bacteria.
COG0010. LUCA.
KOiK01479.
OMAiVARNKGR.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
HAMAPiMF_00737. Formimidoylglutam. 1 hit.
InterProiIPR005923. HutG.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01227. hutG. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KSQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNFTTEHT WQGRHDPEDG QAGRRVHHIA CPIQVGELAN QEPGVALIGF
60 70 80 90 100
ECDAGVERNK GRTGAKHAPS LIKQALANLA WHHPIPIYDL GNIRCEGDEL
110 120 130 140 150
EQAQQECAQV IQQALPHARA IVLGGGHEIA WATFQGLAQH FLATGVKQPR
160 170 180 190 200
IGIINFDAHF DLRTFESELA PVRPSSGTPF NQIHHFCQQQ GWDFHYACLG
210 220 230 240 250
VSRASNTPAL FERADKLGVW YVEDKAFSPL SLKDHLTQLQ HFIDDCDYLY
260 270 280 290 300
LTIDLDVFPA ASAPGVSAPA ARGVSLEALA PYFDRILHYK NKLMIADIAE
310 320 330
YNPSFDIDQH TARLAARLCW DIANAMAEQV QSIRHP
Length:336
Mass (Da):37,329
Last modified:October 1, 2000 - v1
Checksum:iEBC94AF053A98696
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94363.1.
PIRiG82228.
RefSeqiNP_230849.1. NC_002505.1.
WP_001069038.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF94363; AAF94363; VC_1204.
GeneIDi2614637.
KEGGivch:VC1204.
PATRICi20081496. VBIVibCho83274_1151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94363.1.
PIRiG82228.
RefSeqiNP_230849.1. NC_002505.1.
WP_001069038.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XFKX-ray1.80A1-336[»]
ProteinModelPortaliQ9KSQ2.
SMRiQ9KSQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1204.

Protocols and materials databases

DNASUi2614637.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF94363; AAF94363; VC_1204.
GeneIDi2614637.
KEGGivch:VC1204.
PATRICi20081496. VBIVibCho83274_1151.

Phylogenomic databases

eggNOGiENOG41088SP. Bacteria.
COG0010. LUCA.
KOiK01479.
OMAiVARNKGR.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00552.
BioCyciVCHO:VC1204-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KSQ2.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
HAMAPiMF_00737. Formimidoylglutam. 1 hit.
InterProiIPR005923. HutG.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01227. hutG. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHUTG_VIBCH
AccessioniPrimary (citable) accession number: Q9KSQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.